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Structure paper

TitleArchitecture and assembly mechanism of native glycine receptors.
Journal, issue, pagesNature, Vol. 599, Issue 7885, Page 513-517, Year 2021
Publish dateSep 23, 2021
AuthorsHongtao Zhu / Eric Gouaux /
PubMed AbstractGlycine receptors (GlyRs) are pentameric, 'Cys-loop' receptors that form chloride-permeable channels and mediate fast inhibitory signalling throughout the central nervous system. In the spinal cord ...Glycine receptors (GlyRs) are pentameric, 'Cys-loop' receptors that form chloride-permeable channels and mediate fast inhibitory signalling throughout the central nervous system. In the spinal cord and brainstem, GlyRs regulate locomotion and cause movement disorders when mutated. However, the stoichiometry of native GlyRs and the mechanism by which they are assembled remain unclear, despite extensive investigation. Here we report cryo-electron microscopy structures of native GlyRs from pig spinal cord and brainstem, revealing structural insights into heteromeric receptors and their predominant subunit stoichiometry of 4α:1β. Within the heteromeric pentamer, the β(+)-α(-) interface adopts a structure that is distinct from the α(+)-α(-) and α(+)-β(-) interfaces. Furthermore, the β-subunit contains a unique phenylalanine residue that resides within the pore and disrupts the canonical picrotoxin site. These results explain why inclusion of the β-subunit breaks receptor symmetry and alters ion channel pharmacology. We also find incomplete receptor complexes and, by elucidating their structures, reveal the architectures of partially assembled α-trimers and α-tetramers.
External linksNature / PubMed:34555840 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 12.0 Å
Structure data

23910

7mlu

EMDB-23910, PDB-7mlu:
Cryo-EM reveals partially and fully assembled native glycine receptors,homomeric pentamer
Method: EM (single particle) / Resolution: 4.1 Å

23911

7mlv

EMDB-23911, PDB-7mlv:
Cryo-EM reveals partially and fully assembled native glycine receptors,homomeric tetramer
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-23912:
Cryo-EM reveals partially and fully assembled native glycine receptors, homomeric trimer
Method: EM (single particle) / Resolution: 12.0 Å

23913

7mly

EMDB-23913, PDB-7mly:
Cryo-EM reveals partially and fully assembled native glycine receptors,heteromeric pentamer
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-BMA:
beta-D-mannopyranose

ChemComp-HP6:
HEPTANE

ChemComp-DD9:
nonane

ChemComp-LNK:
PENTANE

ChemComp-MYS:
PENTADECANE

ChemComp-D10:
DECANE

ChemComp-NBU:
N-BUTANE

ChemComp-GLY:
GLYCINE

ChemComp-D12:
DODECANE

ChemComp-OCT:
N-OCTANE

ChemComp-HEX:
HEXANE

ChemComp-UND:
UNDECANE

Source
  • sus scrofa (pig)
  • rattus norvegicus (Norway rat)
  • Pig (pig)
KeywordsMEMBRANE PROTEIN / SIGNALING PROTEIN / glycine receptor / ion channel / homomeric pentamer / homomeric tetramer / heteromeric pentamer

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